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TPST1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O60507 |
|---|---|
| Clone Names | 3111904 |
| Gene ID | 8460 |
|---|---|
| Other Names | Protein-tyrosine sulfotransferase 1, Tyrosylprotein sulfotransferase 1, TPST-1, TPST1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2321a was selected from the N-term region of human TPST1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | TPST1 |
|---|---|
| Function | Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. |
| Cellular Location | Golgi apparatus membrane; Single-pass type II membrane protein |
| Tissue Location | Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
The importance of tyrosine O-sulfation in protein-protein interactions is illustrated by the sulfation of tyrosine residues in the leukocyte adhesion molecule P-selectin glycoprotein ligand-1; sulfation is required for its binding to P-selectin on activated endothelium. This enzyme represents a new class of Golgi sulfotransferases that catalyze tyrosine O-sulfation of many protein substrates involved in diverse physiologic functions including inflammation, hemostasis, body weight and reproductive physiology.
References
Hillier, L.W., et al., Nature 424(6945):157-164 (2003).Scherer, S.W., et al., Science 300(5620):767-772 (2003).Seibert, C., et al., Proc. Natl. Acad. Sci. U.S.A. 99(17):11031-11036 (2002).Goettsch, S., et al., Biochem. Biophys. Res. Commun. 294(3):541-546 (2002).Popovic, M., et al., Eur. J. Hum. Genet. 10(4):250-258 (2002).
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